Function Since antibodies exist freely in the bloodstream, they are said to be part of the humoral immune system. Circulating antibodies are produced by clonal B cells that specifically respond to only one antigen (an example is a virus capsid protein fragment) . Antibodies contribute to immunity in three main ways: they can prevent pathogens from entering or damaging cells by binding to them; they can stimulate removal of a pathogen by macrophages and other cells by coating the pathogen; and they can trigger direct pathogen destruction by stimulating other immune responses such as the complement pathway. Antibodies that bind to surface antigens on, for example a bacterium, attract the first component of the complement cascade with their Fc region and initiate activation of the "classical" complement system. This results in the killing of bacteria in two ways. First, the binding of the antibody and complement molecules marks the microbe for ingestion by phagocytes in a process called opsonization; these phagocytes are attracted by certain complement molecules generated in the complement cascade. Secondly, some complement system components form a membrane attack complex to assist antibodies to kill the bacterium directly. To combat pathogens that replicate outside cells, antibodies bind to pathogens to link them together, causing them to agglutinate. Since an antibody has at least two paratopes it can bind more than one antigen by binding identical epitopes carried on the surfaces of these antigens. By coating the pathogen, antibodies stimulate effector functions against the pathogen in cells that recognize their Fc region. Those cells which recognize coated pathogens have Fc receptors which, as the name suggests, interacts with the Fc region of IgA, IgG, and IgE antibodies. The engagement of a particular antibody with the Fc receptor on a particular cell triggers an effector function of that cell; phagocytes will phagocytose, mast cells and neutrophils will degranulate, natural killer cells will release cytokines and cytotoxic molecules; that will ultimately result in destruction of the invading microbe. The Fc receptors are isotype-specific, which gives greater flexibility to the immune system, invoking only the appropriate immune mechanisms for distinct pathogens.
Antigens
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Taking a vaccination - you are enabling your body to produce antibodies. Taking antibodies - you get antibodies, but they eventually disappear from your blood stream, and without them being replenished by your own cells, you lose the protection.
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Antibodies are made by a type of white blood cell called B cells. When the body detects the presence of a foreign substance (antigen), B cells are activated to produce antibodies specific to that antigen. These antibodies work to help the immune system recognize and eliminate the invader.
Antibodies attach to antigens, which are foreign substances such as viruses or bacteria, to make them harmless by marking them for destruction by the immune system.
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Pathogens such as bacteria, viruses, fungi, and parasites can respond to antibodies produced by the immune system. Antibodies work by binding to specific antigens on the surface of pathogens, marking them for destruction by other immune cells. This antibody response is a key component of the adaptive immune system's defense mechanism against infections.
White blood cells produce antibodies to diseases. The antibodies enter the bloodstream and prevent a specific disease from recurring. One type of white blood cells, called B cells, manufacture and release the antibodies. Another type, called T cells, does the job of penetrating the infected cells so that the antibodies can do their work.
Vaccines stimulate production of antibodies.
Antibodies
No, not all antibodies can work with any antigen. Antibodies are highly specific in recognizing and binding to a particular antigen based on their unique binding sites. The binding of an antibody to an antigen is based on complementary shapes and charges, so a specific antibody will only bind to a specific antigen that matches its binding site.